Isolation and amino acid sequence of a novel 6.8-kDa mitochondrial proteolipid from beef heart. Use of FAB-MS for molecular mass determination.
We have isolated a 6.8 kDa proteolipid from an acidic chloroform/methanol extract of bovine cardiac muscle. The molecular mass of the polypeptide was measured by fast atom bombardment-mass spectrometry (FAB-MS) (m/z6834.1). Its amino acid sequence was partly determined by direct sequencing and completed by characterization of cyanogen bromide and tryptic fragments (sequencing, FAB-MS and amino acid analysis). The polypeptide consists of 60 amino acid residues. Polyclonal antibodies raised in rabbit allowed its localization by electroimmunoblotting in mitochondria.
Terzi
E
E
Laboratoire de Chimie Organique des Substances Naturelles, URA CNRS 31, Strasbourg, France.
Boyot
P
P
Van Dorsselaer
A
A
Luu
B
B
Trifilieff
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D015151:Immunoblotting; D013058:Mass Spectrometry; D008929:Mitochondria, Heart / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification; D011510:Proteolipids / Q000302:isolation & purification*; D012997:Solvents
D010446:Peptide Fragments; D010455:Peptides; D011510:Proteolipids; D012997:Solvents